QUANTITATIVE COMPARISON OF SHEAR-DEPENDENT STAPHYLOCOCCUS-AUREUS ADHESION TO 3 POLYURETHANE IONOMER ANALOGS WITH DISTINCT SURFACE-PROPERTIES

Citation
Rb. Dickinson et al., QUANTITATIVE COMPARISON OF SHEAR-DEPENDENT STAPHYLOCOCCUS-AUREUS ADHESION TO 3 POLYURETHANE IONOMER ANALOGS WITH DISTINCT SURFACE-PROPERTIES, Journal of biomedical materials research, 36(2), 1997, pp. 152-162
Citations number
46
Categorie Soggetti
Engineering, Biomedical","Materials Science, Biomaterials
ISSN journal
00219304
Volume
36
Issue
2
Year of publication
1997
Pages
152 - 162
Database
ISI
SICI code
0021-9304(1997)36:2<152:QCOSSA>2.0.ZU;2-1
Abstract
Bacterial adhesion is a central step in infection on biomaterial surfa ces; however, the relation between biomaterial surface properties and adhesion remains poorly understood. To quantitatively determine the re lationship among polyurethane surface properties, protein coating, and adhesion, we have compared attachment and detachment kinetics of Stap hylococcus aureus on three different novel polyurethanes with differen t protein coatings. Rate constants for attachment or detachment were m easured as a function of shear rate in a well-defined laminar flow fie ld. The tested polyurethanes included a relatively hydrophobic-base po lyether urethane and hydrophilic anionomer and cationomer analogs of t he base material. Materials were tested bare, or coated with human fib rinogen, plasma, or albumin. The results suggest that the presence of fibrinogen or plasma greatly enhance the attachment rate constants and decrease the detachment rate constants on all materials. The most ext reme differences among the different materials were observed on the ba re materials, with the base polyurethane being most resistant to both attachment and detachment. However, except for a reduced attachment ra te constant on the plasma-coated sulfonated polyurethane, few differen ces in the rate constants were observed among protein-coated materials , suggesting the primary role of surface properties is masked by the p resence of the adsorbed protein layer. (C) 1997 John Wiley & Sons, Inc .